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Database: UniProt
Entry: F6W5N4_CALJA
LinkDB: F6W5N4_CALJA
Original site: F6W5N4_CALJA 
ID   F6W5N4_CALJA            Unreviewed;      1285 AA.
AC   F6W5N4;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 4.
DT   27-MAR-2024, entry version 73.
DE   RecName: Full=mitogen-activated protein kinase kinase kinase {ECO:0000256|ARBA:ARBA00012406};
DE            EC=2.7.11.25 {ECO:0000256|ARBA:ARBA00012406};
GN   Name=MAP3K6 {ECO:0000313|Ensembl:ENSCJAP00000016893.5};
OS   Callithrix jacchus (White-tufted-ear marmoset).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC   Callitrichinae; Callithrix; Callithrix.
OX   NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000016893.5, ECO:0000313|Proteomes:UP000008225};
RN   [1] {ECO:0000313|Ensembl:ENSCJAP00000016893.5}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSCJAP00000016893.5}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.25;
CC         Evidence={ECO:0000256|ARBA:ARBA00000478};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.25; Evidence={ECO:0000256|ARBA:ARBA00000106};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC       protein kinase family. MAP kinase kinase kinase subfamily.
CC       {ECO:0000256|ARBA:ARBA00006529}.
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DR   STRING; 9483.ENSCJAP00000016893; -.
DR   Ensembl; ENSCJAT00000017861.5; ENSCJAP00000016893.5; ENSCJAG00000009171.5.
DR   eggNOG; KOG4279; Eukaryota.
DR   GeneTree; ENSGT00940000159398; -.
DR   HOGENOM; CLU_003687_3_0_1; -.
DR   InParanoid; F6W5N4; -.
DR   OMA; VEQLLHC; -.
DR   TreeFam; TF105115; -.
DR   Proteomes; UP000008225; Chromosome 7.
DR   Bgee; ENSCJAG00000009171; Expressed in kidney and 6 other cell types or tissues.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:Ensembl.
DR   GO; GO:0004709; F:MAP kinase kinase kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd06624; STKc_ASK; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR046872; DRHyd-ASK.
DR   InterPro; IPR046873; HisK-N-like.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR043969; MAP3K_PH.
DR   InterPro; IPR025136; MAP3K_TRAF-bd.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR013761; SAM/pointed_sf.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR11584:SF391; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 6; 1.
DR   PANTHER; PTHR11584; SERINE/THREONINE PROTEIN KINASE; 1.
DR   Pfam; PF19039; ASK_PH; 1.
DR   Pfam; PF20309; DRHyd-ASK; 1.
DR   Pfam; PF20302; HisK-N-like; 1.
DR   Pfam; PF13281; MAP3K_TRAF_bd; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW   Kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000008225};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022527}.
FT   DOMAIN          648..906
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          900..996
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1127..1153
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        930..948
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1127..1143
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         677
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1285 AA;  142330 MW;  022D5A385B1E3CA6 CRC64;
     MAGPCPRSGA ERAGSCWQDP LAEALSRGRP LATPPGRGCA RSRPLSVVYV LTREPQPGLE
     PREGTEAEPL LLRCLREACA QLPGPRPPPQ LLSLPFGTLA LGDTAALDAF YNADVVVLEV
     SSSLAQPSLF YHLGVRESFS MTNNVLLCSQ ADLPDLQALR EDVFQKNSDC VGSYTLIPYV
     VMATGRVLCG DAGLLRGLAD GLVQAGVGTE ALLTPLVSRL ARLLEATPTD SCGYFRETIR
     RDIRQARERF SGPQLRQELA RLQRRLDSVE LLSPDIVMNL LLSYRDVQDY SAIIELVETL
     QALPTCDVAA QHNVCFHYTF ALNRRNRPGD RTKALAVLLP LVQLEGSVAP DLYCMCGRIY
     KDMFFGSGFQ DAGHREQAYH WYRKAFDVEP SLHSGINAAV LLIAAGQHFE DSKELRLIGM
     KLGCLLARKG CVEKMQYYWD VGFYLGAQIL ADDPTQVVLA AEQLYKLNAP IWYLVSVMET
     FLLYQHFRPT PEPPAGPPRR AHFWLHFLLQ SCQPFKTACP QGDQCLVLVL EMNKVLLPAK
     LKVQGTDPVS TVTLSLLEPE TQDIPSSWTF PVASICGVST SKRDERCCFL YALPPAQDVQ
     LCFPSVGHCQ WFCSLIQALV TNPDSTAPAE EAEGVGEVLE FDYEYTETGE RLVLGKGTYG
     VVYAGRDRHT RVRIAIKEIP ERDSRFSQPL HEEIALHKRL RHKNIVRYLG SASQDGYLKI
     FMEEVPGGSL SSLLRSVWGP LKDNESTISF YTRQILQGLG YLHDNHIVHR DIKGDNVLIN
     TFSGLLKISD FGTSKRLAGI TPCTETFTGT LQYMAPEIID QGPRGYGKAA DIWSLGCTVI
     EMATGHPPFH ELGSPQAAMF QVGMYKVHPP MPSSLSAEAQ AFLLRTFEPD PRLRASAQAL
     LGDPFLQPGK RSRSPSSPRH APQPSDAPSA SPTPSADSTT QSQTLPCPQA PSQHPPNPPK
     RCLSFGGTSQ LRVPEEPAAE EPASPEESSG LSLLHQESKR RAMLAAVLEQ ELPALAENLH
     QEQEQVSRLG RNHVEQLLRC LGAHIHTPNR RHLAQELRVL QGRLRAQGLG PALLHAPLFA
     FPDVVKQILR RRQIRPHWMF VLDSLLSRAV RAALAVLGQE VEKEVVSPRS EELRKEGDSR
     QRPLPVEPEQ GPPPLLVQLS LLRAETDRLR EVLAGKEREY QALVQRALQR VNEEAGTCAR
     ASEPPAALSM DQGLVQWLQE LNVDSGTIQM LLNHSFTLHI LLTYATRDDL VYTRIRGGMV
     CRIWRAILAQ RTESTSVTPG PWKAE
//
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